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Protein

Adaptin ear-binding coat-associated protein 1

Gene

Necap1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in endocytosis.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Adaptin ear-binding coat-associated protein 1
Alternative name(s):
NECAP endocytosis-associated protein 1
Short name:
NECAP-1
Gene namesi
Name:Necap1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1306053. Necap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Adaptin ear-binding coat-associated protein 1PRO_0000213070Add
BLAST

Proteomic databases

PaxDbiP69682.
PRIDEiP69682.

PTM databases

iPTMnetiP69682.

Expressioni

Tissue specificityi

Expressed predominantly in brain (at protein level).1 Publication

Gene expression databases

GenevisibleiP69682. RN.

Interactioni

Subunit structurei

Interacts with AP1G1 and AP2A1 components of the adapter protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins GGA1, GGA2 and GGA3 (By similarity). Interacts with AP2A2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMPHP494183EBI-7592718,EBI-7121510From a different organism.

Protein-protein interaction databases

BioGridi300059. 9 interactions.
DIPiDIP-44064N.
IntActiP69682. 4 interactions.
MINTiMINT-5260811.
STRINGi10116.ENSRNOP00000013272.

Structurei

3D structure databases

ProteinModelPortaliP69682.
SMRiP69682. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi254 – 2574WXXF motif 1
Motifi274 – 2774WXXF motif 2

Domaini

The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself. The WXXF motif 1, which is preceded by an acidic residue and has a glycine in second position mediates specific interaction with AP-1. The WXXF motif 2, which is followed by the C-terminal carboxyl group negative charge, allows specific interaction with AP-2.2 Publications

Sequence similaritiesi

Belongs to the NECAP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2500. Eukaryota.
ENOG41113PS. LUCA.
GeneTreeiENSGT00390000009359.
HOGENOMiHOG000231188.
HOVERGENiHBG060621.
InParanoidiP69682.
KOiK20069.
OMAiESQEMDN.
OrthoDBiEOG76X61J.
PhylomeDBiP69682.
TreeFamiTF314482.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012466. NECAP-1_N.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF07933. DUF1681. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.

Sequencei

Sequence statusi: Complete.

P69682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT
60 70 80 90 100
SKGKIAYIKL EDKVSGELFA QAPVEQYPGI AVETVADSSR YFVIRIQDGT
110 120 130 140 150
GRSAFIGIGF TDRGDAFDFN VSLQDHFKWV KQETEISKES QEMDSRPKLD
160 170 180 190 200
LGFKEGQTIK LSIGNITAKK GGTSKPRASG TGGLSLLPPP PGGKVTIPPP
210 220 230 240 250
SSSVAISNHV TPPPIPKSNH GSNDSDILLD LDSPAPVPTS APAPAPASTS
260 270
NDLWGDFSTA SSSVPNQAPQ PSNWVQF
Length:277
Mass (Da):29,792
Last modified:March 29, 2005 - v1
Checksum:iF8DCDABF95C838C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03032682 Genomic DNA. No translation available.
BC097496 mRNA. Translation: AAH97496.1.
RefSeqiNP_001025090.1. NM_001029919.2.
UniGeneiRn.58356.

Genome annotation databases

EnsembliENSRNOT00000013272; ENSRNOP00000013272; ENSRNOG00000009236.
GeneIDi312694.
KEGGirno:312694.
UCSCiRGD:1306053. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03032682 Genomic DNA. No translation available.
BC097496 mRNA. Translation: AAH97496.1.
RefSeqiNP_001025090.1. NM_001029919.2.
UniGeneiRn.58356.

3D structure databases

ProteinModelPortaliP69682.
SMRiP69682. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi300059. 9 interactions.
DIPiDIP-44064N.
IntActiP69682. 4 interactions.
MINTiMINT-5260811.
STRINGi10116.ENSRNOP00000013272.

PTM databases

iPTMnetiP69682.

Proteomic databases

PaxDbiP69682.
PRIDEiP69682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013272; ENSRNOP00000013272; ENSRNOG00000009236.
GeneIDi312694.
KEGGirno:312694.
UCSCiRGD:1306053. rat.

Organism-specific databases

CTDi25977.
RGDi1306053. Necap1.

Phylogenomic databases

eggNOGiKOG2500. Eukaryota.
ENOG41113PS. LUCA.
GeneTreeiENSGT00390000009359.
HOGENOMiHOG000231188.
HOVERGENiHBG060621.
InParanoidiP69682.
KOiK20069.
OMAiESQEMDN.
OrthoDBiEOG76X61J.
PhylomeDBiP69682.
TreeFamiTF314482.

Miscellaneous databases

PROiP69682.

Gene expression databases

GenevisibleiP69682. RN.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012466. NECAP-1_N.
IPR011993. PH_dom-like.
[Graphical view]
PfamiPF07933. DUF1681. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 103-128 AND 161-169, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Identification of a family of endocytic proteins that define a new alpha-adaptin ear-binding motif."
    Ritter B., Philie J., Girard M., Tung E.C., Blondeau F., McPherson P.S.
    EMBO Rep. 4:1089-1095(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH AP1G1 AND AP2A1.
  5. "Dual engagement regulation of protein interactions with the AP-2 adaptor alpha appendage."
    Mishra S.K., Hawryluk M.J., Brett T.J., Keyel P.A., Dupin A.L., Jha A., Heuser J.E., Fremont D.H., Traub L.M.
    J. Biol. Chem. 279:46191-46203(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, INTERACTION WITH AP2A2.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNECP1_RAT
AccessioniPrimary (citable) accession number: P69682
Secondary accession number(s): Q4QR67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: June 8, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.